Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor

HIGHLIGHTS

• who: Charles Bayly-Jones from the Kinetic analysis The determination of enzymatic activity was based on the cleavage of the fluorescent peptide substrate Abz-YVADAPK(Dnp)G-OHMeasurement of kinetic parameters was performed in , well black plates in a volume of , u00b5l (assay buffer , mM HEPES, mM NaCl, pH, .4, .05% Brij). Enzyme solution in buffer was applied and subsequently substituted with inhibitor/DMSO normalisation (Digital Dispenser, e, Tecan, Switzerland) and preincubated at , u00b0C for , min. After addition of substrate reaction was measured at excitation/emission wavelength, nm on a plate reader (Clariostar, BMG Labtech, Germany). For . . .
  

   

  

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